ID A0A165QQV3_EXIGL Unreviewed; 685 AA.
AC A0A165QQV3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein {ECO:0000259|PROSITE:PS50862};
GN ORFNames=EXIGLDRAFT_709477 {ECO:0000313|EMBL:KZW03952.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW03952.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW03952.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW03952.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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DR EMBL; KV425882; KZW03952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QQV3; -.
DR STRING; 1314781.A0A165QQV3; -.
DR InParanoid; A0A165QQV3; -.
DR OrthoDB; 1046261at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd04317; EcAspRS_like_N; 1.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR047089; Asp-tRNA-ligase_1_N.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 257..659
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 75958 MW; A2C7047DEE1CC99E CRC64;
MADGECKRDG SPHVGHGARE HAHERGEDVA RLLVARSELE RAHMLGKACV TRKREHSALS
GAGEHDMSVE LTLGDVGESA RGERERDEVA GPDEGADDVD RLYGSHHCAQ LSAADAGKQV
LLAGWILPER PVSKSFSFFP LKDANGSTQL VAFKPKKDAP ENTRNVLAEL SQVPVESTVL
IEGEVVLRPQ NAVRPEPAGD IEVHVRDFTL LNPALREHMP FIPSSHTGDN LPNEELRLKH
RYLDLRRPQL AANIRKRSQV AHVVRNFLHE CDFVEVETPV LLQSSPEGAR EFLVPSRTSS
SDDEPRFYAL SQSPQQPKQL LVCSGAVDRY FQLARCFRDE DGRRDRQPEF TQIDLEMAFV
SWRPPQSERD NSGWRVGGSE IRDVVQNMLR TVFALDGIAL PELFPVLRYQ EAMAKYGSDK
PDTRFRLQIQ DVTVLLPEAE RAAAAEADSA RTRRSHKHNS LCKPTSSAHL TCALAETLKL
EPGDTIWIST RPRVATAAER EGALCGRIAC LIGLWTPPRE PALLWVTEFP LFTRADEDKD
LLAHGRWSSS HHPFTAPMVE DLPLLASGDF AKIRGQHFDL VLNGYEIGGG SVRVHDPQMQ
ERILRDVLEL SDTECATFAH LLAALRSGAP PHGGMALGFD RFMAILCNTR SIRDVIAFPK
TAGGADLLFN SPSPVAREVL KQYGL
//
